CRLS1: Cardiolipin Synthase 1
Mitochondrial enzyme critical for cardiolipin biosynthesis and mitochondrial membrane integrity
Gene Information Card
| Symbol | CRLS1 |
|---|---|
| Full Name | Cardiolipin Synthase 1 |
| Gene Type | Protein coding |
| Chromosomal Location | 20p12.3 |
| NCBI Gene ID | 54675 ncbi.nlm.nih.gov/gene/54675 |
| Ensembl ID | ENSG00000101204 |
| UniProt ID | Q9UJA2 |
| OMIM ID | 608188 |
| HGNC ID | 16148 |
| Aliases | CLS, CLS1, C20orf155, dJ434O11.1 |
Description
CRLS1 encodes cardiolipin synthase 1, a mitochondrial inner membrane enzyme that catalyzes the final step of cardiolipin biosynthesis: the transfer of a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol. Cardiolipin is a unique phospholipid essential for mitochondrial cristae structure, oxidative phosphorylation, and apoptosis. CRLS1 is ubiquitously expressed with highest levels in heart, skeletal muscle, and liver. Mutations in CRLS1 are associated with mitochondrial dysfunction and have been implicated in Barth syndrome-like phenotypes.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Barth syndrome (phenocopy) | Impaired cardiolipin remodeling due to CRLS1 deficiency disrupts mitochondrial membrane integrity and electron transport chain function. | ClinVar, OMIM |
| Mitochondrial complex I deficiency | Reduced cardiolipin levels impair assembly and stability of respiratory chain supercomplexes. | NCBI Gene, PubMed |
| Cardiomyopathy | Cardiolipin deficiency in cardiac mitochondria leads to energy depletion and contractile dysfunction. | OMIM, ClinVar |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Heart | 28.5 | High |
| Skeletal muscle | 22.1 | High |
| Liver | 18.3 | High |
| Kidney | 12.7 | Medium |
| Brain | 9.4 | Medium |
| Lung | 6.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 15.3 | Cervical cancer cell line |
| HepG2 | 14.8 | Hepatocellular carcinoma |
| K562 | 11.2 | Leukemia cell line |
| SH-SY5Y | 9.7 | Neuroblastoma |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1A>G (p.Met1?) | Missense | <0.01% | Loss of start codon; predicted loss of function |
| c.238C>T (p.Arg80Trp) | Missense | <0.01% | Impaired catalytic activity; reduced cardiolipin synthesis |
| c.497G>A (p.Arg166Gln) | Missense | <0.01% | Decreased enzyme stability; associated with mitochondrial disease |
Mutation functional classification
Loss of Function (LOF)
Missense mutations (e.g., p.Arg80Trp) reduce or abolish cardiolipin synthase activity, leading to cardiolipin deficiency and mitochondrial dysfunction.
Gain of Function (GOF)
No gain-of-function mutations reported in CRLS1.
Dominant Negative (DN)
No dominant-negative mutations reported; CRLS1 is thought to function as a homodimer, but dominant-negative effects have not been documented.
View complete mutation data：
Gene Ontology (GO)
Pathways
• Cardiolipin biosynthesis (Reactome: R-HSA-1483206)
• Glycerophospholipid biosynthesis (KEGG: map00564)
• Mitochondrial biogenesis (WikiPathways: WP126)
Protein Summary
CRLS1 is a 301-amino acid mitochondrial inner membrane protein that functions as a cardiolipin synthase. It catalyzes the condensation of CDP-diacylglycerol and phosphatidylglycerol to form cardiolipin, a dimeric phospholipid essential for mitochondrial function. The enzyme is highly conserved across eukaryotes. CRLS1 deficiency leads to reduced cardiolipin levels, impaired mitochondrial respiration, and increased reactive oxygen species. The protein contains a conserved catalytic domain and is predicted to form homodimers. Post-translational modifications include phosphorylation at Ser-237, which may regulate activity.
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